1NDH
CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004128 | molecular_function | cytochrome-b5 reductase activity, acting on NAD(P)H |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005741 | cellular_component | mitochondrial outer membrane |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006695 | biological_process | cholesterol biosynthetic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016126 | biological_process | sterol biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FAD A 273 |
| Chain | Residue |
| A | ARG63 |
| A | LYS91 |
| A | GLY95 |
| A | GLY96 |
| A | LYS97 |
| A | MET98 |
| A | SER99 |
| A | THR153 |
| A | THR156 |
| A | HOH276 |
| A | HOH277 |
| A | PRO64 |
| A | HOH279 |
| A | HOH284 |
| A | TYR65 |
| A | THR66 |
| A | ILE81 |
| A | LYS82 |
| A | VAL83 |
| A | PHE85 |
| A | LYS86 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 112 |
| Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00716","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7893687","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NDH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00387","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00387","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00387","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCN2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details |
| Chain | Residue | Details |
| A | TYR65 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 862 |
| Chain | Residue | Details |
| A | HIS49 | proton shuttle (general acid/base), single electron shuttle |
| A | TYR65 | electrostatic stabiliser |
| A | THR66 | proton shuttle (general acid/base), single electron shuttle |
| A | CYS245 | alter redox potential |
